ID F0ZH80_DICPU Unreviewed; 1335 AA.
AC F0ZH80;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN ORFNames=DICPUDRAFT_54488 {ECO:0000313|EMBL:EGC36675.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36675.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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DR EMBL; GL871019; EGC36675.1; -; Genomic_DNA.
DR RefSeq; XP_003286774.1; XM_003286726.1.
DR STRING; 5786.F0ZH80; -.
DR EnsemblProtists; EGC36675; EGC36675; DICPUDRAFT_54488.
DR GeneID; 10504168; -.
DR KEGG; dpp:DICPUDRAFT_54488; -.
DR eggNOG; KOG1337; Eukaryota.
DR InParanoid; F0ZH80; -.
DR OMA; NFLWARS; -.
DR OrthoDB; 1219891at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR CDD; cd10527; SET_LSMT; 1.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR13271:SF155; CYTOCHROME C LYSINE N-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 818..1035
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1062..1089
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 32..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 153132 MW; B9F22F95063F350A CRC64;
MESYDKSSTE VNEDGVDGLV KEFEKEGMKL NSKRVSLSSS TGISNTPPNT SPPINSSIQL
QQQSQQSNFN PLSVSNNLMP QISPFILGYA REDMSKDDEL AIIPSYLMPL HPFACYHSLN
FLLDYFKQSC FYPNTLNNNN NANNNSNKEH LNKSLNEIID NKLQITEALT KVIYKFIYNE
HPELLSRLSI SIDDFVMLLF LVAEYYHNSI IDPLNNTSHS LKKLKSSSLK PAAASQSSFT
PSSATSSTSK SNVANYSYYE ILNNLINIST PLTKSFGTDS EFQKLLNDIG ENDSNNNEES
NSSNFYLKNN YLDLSNDYIQ IKEQLELIFK WIVDFIGFKL FDNVSSQLSG RDPTTLERVK
LINQNNVVKL KSCLFKCYNY IKIASIVNIT LPNISFKGFL PLPHYLIQSN IYKPVKKLST
STPISPLNNS GSSLVTSGSS VLSSDGLERQ RNLFLSSLEQ DDESFSELVA VLKNKLYKDS
PISLENIEII TLEEFNNRTK NNLTKQSQQQ QQPQSQQHPL LYMKQYNYSS SSLRQDDSSI
IDDYQLDLFT NEELLLYYGY TSLEEEMGFI RFEIQVFKSI EQLEKQFTDQ DELDREIRLM
KIKKSILESY LGDLNSSTSS IITTINNSSA VDITVSTSSF KSNKKLVDTI TLKRKEGYYL
DFLSQENILG YNLLELTRLS KLREVESYFY EEGQLSKQIN LRNEMETLVY LSKQLKLVLI
RITSKLNLIS TLLTNNSRDQ LTNSGSIGSY NNNNIFLYEL EKYYKSHLSI IEQSVILLSN
LKNQFTKPTI KSVPFIKPTD EIYRRFENWL KQGGVQFPKL QIANFTDSTG RGVVTTKKVD
EDEVVVSVPR KYLINVDVAK SNPILGPIFE ELHLNDETIL FLFVIYEKEN PNTFWRPFYD
TLPSYFTTSI HYSSTELLEL EGTNLFAETL AVKQQLQAFR DYLFPELSNQ YPDIFPESVF
SWENFLWARS LLDSRAIQLK IDGKIKSCLV PMADMINHHT NAQISERHFD QDSNCFRMVS
SCNIPANNQI FLHYGALQNS DLALYYGFVI PNNIYDSFHV GYELEADEAE EGEESVQELK
KQKDKLLIDH NLSPDSNYLR KDRIPTKNFA CLRVILLTKE EFNPYIDIWN PINLKNETAV
LQTLYQLVLM LLKSFSSTYQ EDQQLLEVMI NKDNDSKNNI DNESVDSNSN NNNNNNNSDN
DNGINIGNIK KNLSSNELSN NNNGNNSDNN NNNSNHNSRD EDDEEYSEDD SESTNSENDL
QSSEQMRMVL QYRIEQKQIL TSTIEKIVLL MEEMGLELPQ SPEASDQEYD DDQDEDFTLS
SDNDEYFSDT NENDD
//
